GlutaredoxinV1, Main, Exploration, bibRecord, 000D04

The thiol-disulfide oxidoreductase system in the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC 125: discovery of a novel disulfide oxidoreductase enzyme.

Identifieur interne : 000D04 ( Main/Exploration ); précédent : 000D03; suivant : 000D05

The thiol-disulfide oxidoreductase system in the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC 125: discovery of a novel disulfide oxidoreductase enzyme.

Auteurs : Stefania Madonna [Italie] ; Rosanna Papa ; Leila Birolo ; Flavia Autore ; Nunzianna Doti ; Gennaro Marino ; Eric Quemeneur ; Giovanni Sannia ; Maria L. Tutino ; Angela Duilio

Source :

Extremophiles : life under extreme conditions [ 1431-0651 ] ; 2006.

RBID : pubmed:16179963

Descripteurs français

English descriptors

KwdEn :
- Adaptation, Physiological (MeSH), Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Cold Temperature (MeSH), DNA, Bacterial (genetics), Enzyme Stability (MeSH), Escherichia coli (genetics), Gene Expression (MeSH), Genes, Bacterial (MeSH), Molecular Sequence Data (MeSH), Protein Disulfide Reductase (Glutathione) (genetics), Protein Disulfide Reductase (Glutathione) (metabolism), Protein Disulfide-Isomerases (genetics), Protein Disulfide-Isomerases (metabolism), Pseudoalteromonas (enzymology), Pseudoalteromonas (genetics), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Seawater (microbiology), Sequence Homology, Amino Acid (MeSH).
MESH :
- chemical , genetics : DNA, Bacterial, Protein Disulfide Reductase (Glutathione), Protein Disulfide-Isomerases, Recombinant Proteins.
- enzymology : Pseudoalteromonas.
- genetics : Escherichia coli, Pseudoalteromonas.
- chemical , metabolism : Protein Disulfide Reductase (Glutathione), Protein Disulfide-Isomerases, Recombinant Proteins.
- microbiology : Seawater.
- Adaptation, Physiological, Amino Acid Sequence, Base Sequence, Cloning, Molecular, Cold Temperature, Enzyme Stability, Gene Expression, Genes, Bacterial, Molecular Sequence Data, Sequence Homology, Amino Acid.

Abstract

In prokaryotes, protein disulfide bond oxidation, reduction and isomerization are catalyzed by members of the thioredoxin superfamily, characterized by the conserved C-X-X-C motif in their active site. Thioredoxins and glutaredoxins contribute to the reducing power in the cytoplasm, while the Dsb system catalyzes disulfide bonds formation in the periplasmic space. This paper addresses the question of disulfide bonds formation in a cold-adapted micro-organism, Pseudoalteromonas haloplanktis TAC 125 (PhTAC125) by characterizing the DsbA system. We found distinctive features respect mesophilic counterparts that highlighted for the first time the occurrence of two adjacent chromosomal DsbA genes organised in a functional operon. The sophisticated transcriptional regulation mechanism that controls the expression of these two genes was also defined. The two DsbA proteins, named PhDsbA and PhDsbA2, respectively, were expressed in Escherichia coli and characterized. Results reported in this paper provide some insights into disulfide bonds formation in a micro organism isolated in the Antarctic sea water.

DOI: 10.1007/s00792-005-0470-3
PubMed: 16179963

Affiliations:

Italie

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000D90
to stream Main, to step Curation: 000D90

Le document en format XML

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<term>Amino Acid Sequence (MeSH)</term>
<term>Base Sequence (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Cold Temperature (MeSH)</term>
<term>DNA, Bacterial (genetics)</term>
<term>Enzyme Stability (MeSH)</term>
<term>Escherichia coli (genetics)</term>
<term>Gene Expression (MeSH)</term>
<term>Genes, Bacterial (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Protein Disulfide Reductase (Glutathione) (genetics)</term>
<term>Protein Disulfide Reductase (Glutathione) (metabolism)</term>
<term>Protein Disulfide-Isomerases (genetics)</term>
<term>Protein Disulfide-Isomerases (metabolism)</term>
<term>Pseudoalteromonas (enzymology)</term>
<term>Pseudoalteromonas (genetics)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Seawater (microbiology)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>ADN bactérien (génétique)</term>
<term>Adaptation physiologique (MeSH)</term>
<term>Basse température (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Eau de mer (microbiologie)</term>
<term>Escherichia coli (génétique)</term>
<term>Expression des gènes (MeSH)</term>
<term>Gènes bactériens (MeSH)</term>
<term>Protein Disulfide-Isomerases (génétique)</term>
<term>Protein Disulfide-Isomerases (métabolisme)</term>
<term>Protein-disulfide reductase (glutathione) (génétique)</term>
<term>Protein-disulfide reductase (glutathione) (métabolisme)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Pseudoalteromonas (enzymologie)</term>
<term>Pseudoalteromonas (génétique)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Stabilité enzymatique (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Bacterial</term>
<term>Protein Disulfide Reductase (Glutathione)</term>
<term>Protein Disulfide-Isomerases</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Pseudoalteromonas</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN bactérien</term>
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<term>Protein Disulfide-Isomerases</term>
<term>Protein-disulfide reductase (glutathione)</term>
<term>Protéines recombinantes</term>
<term>Pseudoalteromonas</term>
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<term>Protein Disulfide-Isomerases</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Eau de mer</term>
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<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Seawater</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protein Disulfide-Isomerases</term>
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<term>Protéines recombinantes</term>
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<term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Cloning, Molecular</term>
<term>Cold Temperature</term>
<term>Enzyme Stability</term>
<term>Gene Expression</term>
<term>Genes, Bacterial</term>
<term>Molecular Sequence Data</term>
<term>Sequence Homology, Amino Acid</term>
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<term>Basse température</term>
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<term>Données de séquences moléculaires</term>
<term>Expression des gènes</term>
<term>Gènes bactériens</term>
<term>Similitude de séquences d'acides aminés</term>
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<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">In prokaryotes, protein disulfide bond oxidation, reduction and isomerization are catalyzed by members of the thioredoxin superfamily, characterized by the conserved C-X-X-C motif in their active site. Thioredoxins and glutaredoxins contribute to the reducing power in the cytoplasm, while the Dsb system catalyzes disulfide bonds formation in the periplasmic space. This paper addresses the question of disulfide bonds formation in a cold-adapted micro-organism, Pseudoalteromonas haloplanktis TAC 125 (PhTAC125) by characterizing the DsbA system. We found distinctive features respect mesophilic counterparts that highlighted for the first time the occurrence of two adjacent chromosomal DsbA genes organised in a functional operon. The sophisticated transcriptional regulation mechanism that controls the expression of these two genes was also defined. The two DsbA proteins, named PhDsbA and PhDsbA2, respectively, were expressed in Escherichia coli and characterized. Results reported in this paper provide some insights into disulfide bonds formation in a micro organism isolated in the Antarctic sea water.</div>
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<Abstract><AbstractText>In prokaryotes, protein disulfide bond oxidation, reduction and isomerization are catalyzed by members of the thioredoxin superfamily, characterized by the conserved C-X-X-C motif in their active site. Thioredoxins and glutaredoxins contribute to the reducing power in the cytoplasm, while the Dsb system catalyzes disulfide bonds formation in the periplasmic space. This paper addresses the question of disulfide bonds formation in a cold-adapted micro-organism, Pseudoalteromonas haloplanktis TAC 125 (PhTAC125) by characterizing the DsbA system. We found distinctive features respect mesophilic counterparts that highlighted for the first time the occurrence of two adjacent chromosomal DsbA genes organised in a functional operon. The sophisticated transcriptional regulation mechanism that controls the expression of these two genes was also defined. The two DsbA proteins, named PhDsbA and PhDsbA2, respectively, were expressed in Escherichia coli and characterized. Results reported in this paper provide some insights into disulfide bonds formation in a micro organism isolated in the Antarctic sea water.</AbstractText>
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The thiol-disulfide oxidoreductase system in the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC 125: discovery of a novel disulfide oxidoreductase enzyme.

The thiol-disulfide oxidoreductase system in the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC 125: discovery of a novel disulfide oxidoreductase enzyme.

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